PNCA_ECOLI
ID PNCA_ECOLI Reviewed; 213 AA.
AC P21369; P76229; P76910;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Nicotinamidase {ECO:0000303|PubMed:4399474, ECO:0000303|PubMed:8726014};
DE EC=3.5.1.19 {ECO:0000269|PubMed:4399474, ECO:0000305|PubMed:8726014};
DE AltName: Full=Nicotinamide deamidase {ECO:0000303|PubMed:4399474};
DE Short=NAMase {ECO:0000303|PubMed:8726014};
DE AltName: Full=Pyrazinamidase {ECO:0000303|PubMed:8726014};
DE Short=PZAase {ECO:0000303|PubMed:8726014};
DE EC=3.5.1.- {ECO:0000305|PubMed:8726014};
GN Name=pncA {ECO:0000303|PubMed:8726014}; Synonyms=nam, ydjB;
GN OrderedLocusNames=b1768, JW1757;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=2670682; DOI=10.1016/0378-1119(89)90312-0;
RA Jerlstroem P.G., Bezjak D.A., Jennings M.P., Beacham I.R.;
RT "Structure and expression in Escherichia coli K-12 of the L-asparaginase I-
RT encoding ansA gene and its flanking regions.";
RL Gene 78:37-46(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8726014; DOI=10.1128/aac.40.6.1426;
RA Frothingham R., Meeker-O'Connell W.A., Talbot E.A., George J.W.,
RA Kreuzer K.N.;
RT "Identification, cloning, and expression of the Escherichia coli
RT pyrazinamidase and nicotinamidase gene, pncA.";
RL Antimicrob. Agents Chemother. 40:1426-1431(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP PATHWAY.
RC STRAIN=K12;
RX PubMed=4399474; DOI=10.1016/s0021-9258(19)45915-2;
RA Pardee A.B., Benz E.J. Jr., St Peter D.A., Krieger J.N., Meuth M.,
RA Trieshmann H.W. Jr.;
RT "Hyperproduction and purification of nicotinamide deamidase, a
RT microconstitutive enzyme of Escherichia coli.";
RL J. Biol. Chem. 246:6792-6796(1971).
CC -!- FUNCTION: Catalyzes the deamidation of nicotinamide (NAM) into
CC nicotinate (PubMed:4399474, PubMed:8726014). Likely functions in the
CC cyclical salvage pathway for production of NAD from nicotinamide
CC (PubMed:4399474). {ECO:0000269|PubMed:4399474,
CC ECO:0000305|PubMed:8726014}.
CC -!- FUNCTION: Is also able to hydrolyze the first-line antituberculous drug
CC pyrazinamide (PZA) into pyrazinoic acid in vitro, but this reaction is
CC not considered to be physiologically relevant.
CC {ECO:0000305|PubMed:8726014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + nicotinamide = NH4(+) + nicotinate;
CC Xref=Rhea:RHEA:14545, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:32544; EC=3.5.1.19;
CC Evidence={ECO:0000269|PubMed:4399474, ECO:0000305|PubMed:8726014};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyrazinamide = NH4(+) + pyrazine-2-carboxylate;
CC Xref=Rhea:RHEA:35063, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:45285, ChEBI:CHEBI:71266;
CC Evidence={ECO:0000305|PubMed:8726014};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for nicotinamide {ECO:0000269|PubMed:4399474};
CC Vmax=560 umol/min/mg enzyme for the nicotinamidase activity
CC {ECO:0000269|PubMed:4399474};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:4399474};
CC -!- PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate
CC from nicotinamide: step 1/1. {ECO:0000305|PubMed:4399474}.
CC -!- INDUCTION: Is constitutively expressed in very small amounts in E.coli.
CC {ECO:0000269|PubMed:4399474}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR EMBL; M26934; AAA23447.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74838.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15559.1; -; Genomic_DNA.
DR PIR; H64936; QQECA5.
DR RefSeq; NP_416282.4; NC_000913.3.
DR RefSeq; WP_001135066.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P21369; -.
DR SMR; P21369; -.
DR BioGRID; 4262963; 17.
DR DIP; DIP-10520N; -.
DR IntAct; P21369; 5.
DR STRING; 511145.b1768; -.
DR jPOST; P21369; -.
DR PaxDb; P21369; -.
DR PRIDE; P21369; -.
DR EnsemblBacteria; AAC74838; AAC74838; b1768.
DR EnsemblBacteria; BAA15559; BAA15559; BAA15559.
DR GeneID; 946276; -.
DR KEGG; ecj:JW1757; -.
DR KEGG; eco:b1768; -.
DR PATRIC; fig|1411691.4.peg.486; -.
DR EchoBASE; EB1125; -.
DR eggNOG; COG1335; Bacteria.
DR HOGENOM; CLU_068979_13_1_6; -.
DR InParanoid; P21369; -.
DR OMA; DFVDSWP; -.
DR PhylomeDB; P21369; -.
DR BioCyc; EcoCyc:NICOTINAMID-MON; -.
DR BioCyc; MetaCyc:NICOTINAMID-MON; -.
DR UniPathway; UPA00830; UER00790.
DR PRO; PR:P21369; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008936; F:nicotinamidase activity; IDA:EcoCyc.
DR GO; GO:0019365; P:pyridine nucleotide salvage; IMP:EcoCyc.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Pyridine nucleotide biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..213
FT /note="Nicotinamidase"
FT /id="PRO_0000206557"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:I6XD65"
FT ACT_SITE 111
FT /evidence="ECO:0000250|UniProtKB:I6XD65"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:I6XD65"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P53184"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P53184"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P53184"
SQ SEQUENCE 213 AA; 23362 MW; B9F8D946FA18433F CRC64;
MPPRALLLVD LQNDFCAGGA LAVPEGDSTV DVANRLIDWC QSRGEAVIAS QDWHPANHGS
FASQHGVEPY TPGQLDGLPQ TFWPDHCVQN SEGAQLHPLL HQKAIAAVFH KGENPLVDSY
SAFFDNGRRQ KTSLDDWLRD HEIDELIVMG LATDYCVKFT VLDALQLGYK VNVITDGCRG
VNIQPQDSAH AFMEMSAAGA TLYTLADWEE TQG
